MolNFT v1 · #67752 · protein

Crystal structure of a prolyl 4-hydroxylase from bacillus anthracis

3ITQ · Prolyl 4-hydroxylase, alpha subunit domain protein: “Crystal structure of a prolyl 4-hydroxylase from bacillus anthracis”. X-ray diffraction, 1 ligand (PO4), 3 pockets (best druggability 0.46). MolNFT v1 #67752 on GenesisL1: 3D…

PDB: 3ITQ
Type: protein
Length: 394 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prolyl 4-hydroxylase, alpha subunit domain protein
UniProt: Q81LZ8
Ligands: PO4
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prolyl 4-hydroxylase, alpha subunit domain protein	protein	198	23% helix, 33% strand	Q81LZ8
B	Prolyl 4-hydroxylase, alpha subunit domain protein	protein	196	22% helix, 33% strand	Q81LZ8

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.46	0.84	15	GOL
2	120	0.40	0.75	26	empty
3	61	0.26	0.72	18	PO4

Interfaces

1 interface between chains.

A–B · 1198 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3ITQ · Crystal Structure of a Prolyl 4-Hydroxylase from Bacillus anthracis · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q81LZ8
Elsewhere: RCSB PDB 3ITQ · PDBe 3ITQ · UniProt Q81LZ8

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